1gcn

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(New page: 200px<br /><applet load="1gcn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gcn, resolution 3.0&Aring;" /> '''X-RAY ANALYSIS OF GLU...)
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[[Image:1gcn.gif|left|200px]]<br /><applet load="1gcn" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gcn.gif|left|200px]]<br /><applet load="1gcn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gcn, resolution 3.0&Aring;" />
caption="1gcn, resolution 3.0&Aring;" />
'''X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING'''<br />
'''X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING'''<br />
==Overview==
==Overview==
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X-ray analysis of the pancreatic hormone glucagon shows that in crystals, the polypeptide adopts a mainly helical conformation, which is stabilised, by hydrophobic interactions between molecules related by threefold, symmetry. A model is presented in which the glucagon molecule exists in, dilute solutions as an equilibrium population of conformers with little, retention of conformers with little retention of structure, and in which, the helical conformation is stablised by hydrophobic interactions either, as an oligomer or as a complex with the receptor.
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X-ray analysis of the pancreatic hormone glucagon shows that in crystals the polypeptide adopts a mainly helical conformation, which is stabilised by hydrophobic interactions between molecules related by threefold symmetry. A model is presented in which the glucagon molecule exists in dilute solutions as an equilibrium population of conformers with little retention of conformers with little retention of structure, and in which the helical conformation is stablised by hydrophobic interactions either as an oligomer or as a complex with the receptor.
==About this Structure==
==About this Structure==
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1GCN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCN OCA].
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1GCN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCN OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Blundell, T.L.]]
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[[Category: Blundell, T L.]]
[[Category: Dockerill, S.]]
[[Category: Dockerill, S.]]
[[Category: Sasaki, K.]]
[[Category: Sasaki, K.]]
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[[Category: Tickle, I.J.]]
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[[Category: Tickle, I J.]]
[[Category: hormone]]
[[Category: hormone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:56:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:42 2008''

Revision as of 10:48, 21 February 2008


1gcn, resolution 3.0Å

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X-RAY ANALYSIS OF GLUCAGON AND ITS RELATIONSHIP TO RECEPTOR BINDING

Overview

X-ray analysis of the pancreatic hormone glucagon shows that in crystals the polypeptide adopts a mainly helical conformation, which is stabilised by hydrophobic interactions between molecules related by threefold symmetry. A model is presented in which the glucagon molecule exists in dilute solutions as an equilibrium population of conformers with little retention of conformers with little retention of structure, and in which the helical conformation is stablised by hydrophobic interactions either as an oligomer or as a complex with the receptor.

About this Structure

1GCN is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

X-ray analysis of glucagon and its relationship to receptor binding., Sasaki K, Dockerill S, Adamiak DA, Tickle IJ, Blundell T, Nature. 1975 Oct 30;257(5529):751-7. PMID:171582

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